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In vivo localization of radioiodinated peanut lectin in a murine TA3/Ha mammary carcinoma model.

Authors
  • Shysh, A
  • Eu, S M
  • Noujaim, A A
  • Suresh, M R
  • Longenecker, B M
Type
Published Article
Journal
European journal of nuclear medicine
Publication Date
Jan 01, 1985
Volume
10
Issue
1-2
Pages
68–74
Identifiers
PMID: 3979412
Source
Medline
License
Unknown

Abstract

Peanut lectin (PNA) binds avidly to oligosaccharides containing the terminal sequence beta-D-Gal(1----3)alpha-D-GAlNAc. This disaccharide is the immunodeterminant group of the Thomsen-Friedenreich (T) antigen which is present in an exposed form on a number of human and animal adenocarcinomas and can be identified in tumor tissue sections by histochemical PNA staining techniques. We have studied the in vivo uptake of radioiodinated PNA in a murine TA3/Ha mammary adenocarcinoma model to evaluate the potential applications of radiolabeled PNA for the immunodetection of T antigen expressing carcinoma. We have found that PNA has a high in vitro binding affinity for the TA3/Ha tumor cells as well as for epiglycanin, a glycoprotein fraction shed by the TA3/Ha cells. Tissue biodistribution studies after IV 125I-PNA injection into TA3/Ha tumor-bearing mice indicated tumor:blood ratios of 7:1 and 55:1 at 24 and 48 h with corresponding tumor:muscle ratios of 33:1 and 77:1. The high tumor uptake and rapid blood clearance allowed clear scintigraphic delineation of tumor by 24 and 48 h without the necessity for background subtraction techniques. Rapid in vivo deiodination of 125I-PNA also contributed to localization of radioactivity in the stomach, salivary glands, thyroid, and kidney.

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